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P08148

- GP63_LEIMA

UniProt

P08148 - GP63_LEIMA

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Protein

Leishmanolysin

Gene

gp63

Organism
Leishmania major
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Has an integral role during the infection of macrophages in the mammalian host.

Catalytic activityi

Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi264 – 2641Zinc; catalytic
Active sitei265 – 2651
Metal bindingi268 – 2681Zinc; catalytic
Metal bindingi334 – 3341Zinc; catalytic

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM08.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Leishmanolysin (EC:3.4.24.36)
Alternative name(s):
Cell surface protease
Major surface glycoprotein
Major surface protease
Promastigote surface endopeptidase
Protein gp63
Gene namesi
Name:gp63
OrganismiLeishmania major
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi254 – 2541Y → D: No significant effect on protein expression levels or catalytic activity. 1 Publication
Mutagenesisi264 – 2641H → F or Y: No detectable overexpression of mutant protein and hence little catalytic activity. 1 Publication
Mutagenesisi265 – 2651E → D: No significant effect on protein expression levels but almost abolishes catalytic activity. 1 Publication
Mutagenesisi268 – 2681H → N or Y: No detectable overexpression of mutant protein and hence little catalytic activity. 1 Publication
Mutagenesisi300 – 3001N → Q: Increases electrophoretic mobility of the protein. 1 Publication
Mutagenesisi407 – 4071N → Q: Increases electrophoretic mobility of the protein. 1 Publication
Mutagenesisi534 – 5341N → Q: Increases electrophoretic mobility of the protein. 1 Publication
Mutagenesisi577 – 5771N → L: Causes extracellular release of the protein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Sequence AnalysisAdd
BLAST
Propeptidei40 – 10061Activation peptide1 PublicationPRO_0000028667Add
BLAST
Chaini101 – 577477LeishmanolysinPRO_0000028668Add
BLAST
Propeptidei578 – 60225Removed in mature formPRO_0000028669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi125 ↔ 1421 Publication
Disulfide bondi191 ↔ 2301 Publication
Glycosylationi300 – 3001N-linked (GlcNAc...)2 Publications
Disulfide bondi314 ↔ 3861 Publication
Disulfide bondi393 ↔ 4551 Publication
Disulfide bondi406 ↔ 4251 Publication
Glycosylationi407 – 4071N-linked (GlcNAc...)2 Publications
Disulfide bondi415 ↔ 4891 Publication
Disulfide bondi466 ↔ 5101 Publication
Disulfide bondi515 ↔ 5651 Publication
Glycosylationi534 – 5341N-linked (GlcNAc...)1 Publication
Disulfide bondi535 ↔ 5581 Publication
Lipidationi577 – 5771GPI-anchor amidated asparagine1 Publication

Post-translational modificationi

The phosphatidylinositol moiety of the GPI-anchor contains a fully saturated, unbranched 1-O-alkyl chain (mainly C24:0) and a mixture of fully saturated unbranched 2-O-acyl chains (C12:0, C14:0, C16:0, and C18:0).

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

PTM databases

UniCarbKBiP08148.

Miscellaneous databases

PMAP-CutDBP08148.

Structurei

Secondary structure

1
602
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi111 – 1144Combined sources
Helixi116 – 1194Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi139 – 1413Combined sources
Helixi144 – 1463Combined sources
Helixi150 – 1589Combined sources
Helixi160 – 16910Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi177 – 1815Combined sources
Helixi191 – 1933Combined sources
Helixi198 – 2025Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi209 – 2157Combined sources
Beta strandi226 – 2327Combined sources
Beta strandi238 – 2447Combined sources
Helixi247 – 2493Combined sources
Helixi256 – 26914Combined sources
Helixi274 – 2796Combined sources
Beta strandi283 – 2875Combined sources
Helixi289 – 2913Combined sources
Beta strandi296 – 2994Combined sources
Helixi302 – 31211Combined sources
Beta strandi320 – 3223Combined sources
Turni328 – 3325Combined sources
Beta strandi333 – 3353Combined sources
Turni337 – 3393Combined sources
Beta strandi346 – 3483Combined sources
Helixi356 – 3649Combined sources
Helixi372 – 3743Combined sources
Turni380 – 3834Combined sources
Helixi386 – 3905Combined sources
Beta strandi393 – 3953Combined sources
Beta strandi398 – 4003Combined sources
Turni402 – 4043Combined sources
Beta strandi420 – 4256Combined sources
Helixi435 – 4373Combined sources
Beta strandi440 – 4423Combined sources
Turni450 – 4545Combined sources
Beta strandi458 – 4658Combined sources
Helixi470 – 4723Combined sources
Turni475 – 4773Combined sources
Helixi478 – 4803Combined sources
Beta strandi487 – 4948Combined sources
Beta strandi506 – 51611Combined sources
Turni517 – 5204Combined sources
Beta strandi521 – 5255Combined sources
Beta strandi540 – 5423Combined sources
Helixi543 – 5453Combined sources
Beta strandi548 – 5503Combined sources
Beta strandi555 – 5573Combined sources
Helixi561 – 5655Combined sources
Helixi569 – 5724Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LMLX-ray1.86A100-577[»]
ProteinModelPortaliP08148.
SMRiP08148. Positions 100-574.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08148.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M8 family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR001577. Peptidase_M8.
[Graphical view]
PANTHERiPTHR10942. PTHR10942. 1 hit.
PfamiPF01457. Peptidase_M8. 1 hit.
[Graphical view]
PRINTSiPR00782. LSHMANOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08148-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MSVDSSSTHR RRCVAARLVR LAAAGAAVTV AVGTAAAWAH AGALQHRCVH
60 70 80 90 100
DAMQARVRQS VADHHKAPGA VSAVGLPYVT LDAAHTAAAA DPRPGSARSV
110 120 130 140 150
VRDVNWGALR IAVSTEDLTD PAYHCARVGQ HVKDHAGAIV TCTAEDILTN
160 170 180 190 200
EKRDILVKHL IPQAVQLHTE RLKVQQVQGK WKVTDMVGDI CGDFKVPQAH
210 220 230 240 250
ITEGFSNTDF VMYVASVPSE EGVLAWATTC QTFSDGHPAV GVINIPAANI
260 270 280 290 300
ASRYDQLVTR VVTHEMAHAL GFSGPFFEDA RIVANVPNVR GKNFDVPVIN
310 320 330 340 350
SSTAVAKARE QYGCDTLEYL EVEDQGGAGS AGSHIKMRNA QDELMAPAAA
360 370 380 390 400
AGYYTALTMA IFQDLGFYQA DFSKAEVMPW GQNAGCAFLT NKCMEQSVTQ
410 420 430 440 450
WPAMFCNESE DAIRCPTSRL SLGACGVTRH PGLPPYWQYF TDPSLAGVSA
460 470 480 490 500
FMDYCPVVVP YSDGSCTQRA SEAHASLLPF NVFSDAARCI DGAFRPKATD
510 520 530 540 550
GIVKSYAGLC ANVQCDTATR TYSVQVHGSN DYTNCTPGLR VELSTVSNAF
560 570 580 590 600
EGGGYITCPP YVEVCQGNVQ AAKDGGNTAA GRRGPRAAAT ALLVAALLAV

AL
Length:602
Mass (Da):63,953
Last modified:April 1, 1990 - v2
Checksum:i982EF3245D87C43E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00647 Genomic DNA. Translation: CAA68673.1.
PIRiPL0221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00647 Genomic DNA. Translation: CAA68673.1 .
PIRi PL0221.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LML X-ray 1.86 A 100-577 [» ]
ProteinModelPortali P08148.
SMRi P08148. Positions 100-574.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M08.001.

PTM databases

UniCarbKBi P08148.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P08148.
PMAP-CutDB P08148.

Family and domain databases

InterProi IPR001577. Peptidase_M8.
[Graphical view ]
PANTHERi PTHR10942. PTHR10942. 1 hit.
Pfami PF01457. Peptidase_M8. 1 hit.
[Graphical view ]
PRINTSi PR00782. LSHMANOLYSIN.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of the major surface antigen of leishmania."
    Button L.L., McMaster W.R.
    J. Exp. Med. 167:724-729(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 101-123.
  2. Button L.L., McMaster W.R.
    J. Exp. Med. 171:589-589(1990)
    Cited for: SEQUENCE REVISION.
  3. "Structure of the glycosyl-phosphatidylinositol membrane anchor of the Leishmania major promastigote surface protease."
    Schneider P., Ferguson M.A.J., McConville M.J., Mehlert A., Homans S.W., Bordier C.
    J. Biol. Chem. 265:16955-16964(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR AT ASN-577.
  4. "Posttranslational regulation of a Leishmania HEXXH metalloprotease (gp63). The effects of site-specific mutagenesis of catalytic, zinc binding, N-glycosylation, and glycosyl phosphatidylinositol addition sites on N-terminal end cleavage, intracellular stability, and extracellular exit."
    McGwire B.S., Chang K.-P.
    J. Biol. Chem. 271:7903-7909(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-254; HIS-264; GLU-265; HIS-268; ASN-300; ASN-407; ASN-534 AND ASN-577.
  5. "A unique, terminally glucosylated oligosaccharide is a common feature on Leishmania cell surfaces."
    Funk V.A., Thomas-Oates J.E., Kielland S.L., Bates P.A., Olafson R.W.
    Mol. Biochem. Parasitol. 84:33-48(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-300 AND ASN-407.
  6. "Crystallization and preliminary X-ray diffraction studies of leishmanolysin, the major surface metalloproteinase from Leishmania major."
    Schlagenhauf E., Etges R., Metcalf P.
    Proteins 22:58-66(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-300; ASN-407 AND ASN-534.
  7. "The crystal structure of the Leishmania major surface proteinase leishmanolysin."
    Schlagenhauf E., Etges R., Metcalf P.
    Structure 6:1035-1046(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).

Entry informationi

Entry nameiGP63_LEIMA
AccessioniPrimary (citable) accession number: P08148
Secondary accession number(s): P15906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 1, 1990
Last modified: November 26, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3